RL2_THEVO
ID RL2_THEVO Reviewed; 234 AA.
AC Q97BX4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=TV0331;
GN ORFNames=TVG0334954;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; BA000011; BAB59473.1; -; Genomic_DNA.
DR RefSeq; WP_010916585.1; NC_002689.2.
DR AlphaFoldDB; Q97BX4; -.
DR SMR; Q97BX4; -.
DR STRING; 273116.14324546; -.
DR EnsemblBacteria; BAB59473; BAB59473; BAB59473.
DR GeneID; 1440843; -.
DR KEGG; tvo:TVG0334954; -.
DR eggNOG; arCOG04067; Archaea.
DR HOGENOM; CLU_036235_0_1_2; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 74812at2157; -.
DR PhylomeDB; Q97BX4; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..234
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129730"
FT REGION 195..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 25007 MW; CF44BC8BDF9DC1D1 CRC64;
MGKHIIPQRR GHGSLVYRSP SHRHVVDVKH LKPGEYVVKD IIHAPGRNSP LLELVDSTGK
KVYQIAFTGA YVGQKIVAGN VDTINPGTTT VLANIPDGSY VYNIESSPGD GGEFCRSAGT
FALVVSHGSR VTLKLPSGSM RDFDPRCRAT VGVVAASGII DAPILKAGTH VHYLRSKAKR
PYTVRGVAMN AVNHPHGGGN HQHVGRPSTV GRNAPPGRKV GRLSPKRRKV NGSK
